Abstract
CO2 permeability of plasma membrane intrinsic protein 2 (PIP2) aquaporins of Hordeum vulgare L. was investigated. Five PIP2 members were heterologously expressed in Xenopus laevis oocytes. CO2 permeability was determined by decrease of cytosolic pH in CO2-enriched buffer using a hydrogen ion-selective microelectrode. HvPIP2;1, HvPIP2;2, HvPIP2;3 and HvPIP2;5 facilitated CO2 transport across the oocyte cell membrane. However, HvPIP2;4 that is highly homologous to HvPIP2;3 did not. The isoleucine residue at position 254 of HvPIP2;3 was conserved in PIP2 aquaporins of barley, except HvPIP2;4, which possesses methionine instead. CO2 permeability was lost by the substitution of the Ile254 of HvPIP2;3 by methionine, while water permeability was not affected. These results suggest that PIP2 aquaporins are permeable to CO2. and the conserved isoleucine at the end of the E-loop is crucial for CO2 selectivity.
Keywords
Aquaporin
Barley
Carbon dioxide
Plasma membrane intrinsic protein 2
MeSH Terms
Amino Acid Sequence
Animals
Aquaporins/genetics,metabolism
Biological Transport
Carbon Dioxide/metabolism
Cell Membrane/metabolism
Cell Membrane Permeability
Cytosol/metabolism
Gene Expression
Gene Expression Regulation, Plant
Hordeum/genetics,metabolism
Hydrogen-Ion Concentration
Isoleucine
Models, Molecular
Molecular Sequence Data
Oocytes
Plant Proteins/genetics,metabolism
Plant Roots/genetics,metabolism
Sequence Alignment
Water/metabolism
Xenopus
Chemicals
Aquaporins
Plant Proteins
Isoleucine
Water
Carbon Dioxide
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Mori Izumi C
Institute of Plant Science and Resources, Okayama University, 2-20-1 Chuo, Kurashiki, 710-0046 Japan.
Rhee Jiye
Shibasaka Mineo
Sasano Shizuka
Kaneko Toshiyuki
Horie Tomoaki
Katsuhara Maki
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